Evidence map›Paper›PMID 24351045›Full record

ArticleThe Biochemical journal2014

Structural and functional characterization of NanU, a novel high-affinity sialic acid-inducible binding protein of oral and gut-dwelling Bacteroidetes species.

Chatchawal Phansopa, Sumita Roy, John B Rafferty, C W Ian Douglas, Jagroop Pandhal, Phillip C Wright, David J Kelly, Graham P Stafford

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 41 citations in OpenAlex.

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  12. A surface-exposed GH26 β-mannanase fromThe Journal of biological chemistry · 2019
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  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Chatchawal Phansopa*School of Clinical Dentistry, University of Sheffield, Sheffield S10 2TA, U.K.
Sumita Roy*School of Clinical Dentistry, University of Sheffield, Sheffield S10 2TA, U.K.
John B Rafferty†Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, U.K.
C W Ian Douglas*School of Clinical Dentistry, University of Sheffield, Sheffield S10 2TA, U.K.
Jagroop Pandhal‡Department of Chemical and Biological Engineering, University of Sheffield, Sheffield S1 3JD, U.K.
Phillip C Wright‡Department of Chemical and Biological Engineering, University of Sheffield, Sheffield S1 3JD, U.K.
David J Kelly†Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, U.K.
Graham P Stafford*School of Clinical Dentistry, University of Sheffield, Sheffield S10 2TA, U.K.
University of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D524975/1Biotechnology and Biological Sciences Research Council BB/F004842/1The Dunhill Medical Trust R185/0211
6 · The paper itself

Abstract

Many human-dwelling bacteria acquire sialic acid for growth or surface display. We identified previously a sialic acid utilization operon in Tannerella forsythia that includes a novel outer membrane sialic acid-transport system (NanOU), where NanO (neuraminate outer membrane permease) is a putative TonB-dependent receptor and NanU (extracellular neuraminate uptake protein) is a predicted SusD family protein. Using heterologous complementation of nanOU genes into an Escherichia coli strain devoid of outer membrane sialic acid permeases, we show that the nanOU system from the gut bacterium Bacteroides fragilis is functional and demonstrate its dependence on TonB for function. We also show that nanU is required for maximal function of the transport system and that it is expressed in a sialic acid-responsive manner. We also show its cellular localization to the outer membrane using fractionation and immunofluorescence experiments. Ligand-binding studies revealed high-affinity binding of sialic acid to NanU (Kd ~400 nM) from two Bacteroidetes species as well as binding of a range of sialic acid analogues. Determination of the crystal structure of NanU revealed a monomeric SusD-like structure containing a novel motif characterized by an extended kinked helix that might determine sugar-binding specificity. The results of the present study characterize the first bacterial extracellular sialic acid-binding protein and define a sialic acid-specific PUL (polysaccharide utilization locus).

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsBacteroides fragilisBacteroidetesBiological TransportCrystallography, X-RayEscherichia coliIntestinesMembrane ProteinsMouthMutationN-Acetylneuraminic AcidProtein BindingProtein Structure, SecondaryBacterial Outer Membrane ProteinsBacterial ProteinsMembrane ProteinsN-Acetylneuraminic AcidtonB protein, Bacteria

Identifiers

PMID24351045
PMCPMC3969230
OpenAlexW2041946234

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.